Abstract
The GP63 of the protozoan parasite Leishmania is a highly abundant zinc metallopeptidase, mainly glycosylphosphatidylinositol-anchored to the parasite surface, which contributes to a myriad of well-established functions for Leishmania in the interaction with the mammalian host. However, the role of GP63 in the Leishmania-insect vector interplay is still a matter of controversy. Data from GP63 homologues in insect and plant trypanosomatids strongly suggest a participation of GP63 in this interface, either through nutrient acquisition or through binding to the insect gut receptors. GP63 has also been described in the developmental forms of Trypanosoma cruzi, Trypanosoma brucei and Trypanosoma rangeli that deal with the vector. Here, the available data from GP63 will be analyzed from the perspective of the interaction of trypanosomatids with the invertebrate host.
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Abbreviations
- EC:
-
Enzyme class
- EDTA:
-
Ethylenediaminetetraacetic acid
- EGTA:
-
Ethylene glycol tetraacetic acid
- GIPLs:
-
Glycoinositolphospholipids
- GPI:
-
Glycosylphosphatidylinositol
- GPI-PLC:
-
Glycosylphosphatidylinositol-phospholipase C
- HIV:
-
Human immunodeficiency virus
- LPG:
-
Lipophosphoglycan
- MSP:
-
Major surface peptidase
- PARP:
-
Procyclic acidic repetitive protein
- PSP:
-
Promastigote surface peptidase
- VSG:
-
Glycosylphosphatidylinositol-anchored variant surface protein
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Acknowledgments
This study was supported by grants from the following Brazilian Agencies: Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES), Conselho Nacional de Desenvolvimento Científico e Tecnológico (MCT/CNPq), Fundação de Amparo à Pesquisa no Estado do Rio de Janeiro (FAPERJ) and Fundação Oswaldo Cruz (FIOCRUZ).
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d’Avila-Levy, C.M., Altoé, E.C.F., Uehara, L.A., Branquinha, M.H., Santos, A.L.S. (2014). GP63 Function in the Interaction of Trypanosomatids with the Invertebrate Host: Facts and Prospects. In: Santos, A., Branquinha, M., d’Avila-Levy, C., Kneipp, L., Sodré, C. (eds) Proteins and Proteomics of Leishmania and Trypanosoma. Subcellular Biochemistry, vol 74. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-7305-9_11
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